Effect of Arp2/3 Complex on Sperm Motility and Membrane Structure in Bovine

Lee, June-Sub; Park, Yoo-Jin; Kim, Jin; Rahman, Md. Saidur; Kwon, Woo-Sung; Yoon, Sung-Jae; You, Young-Ah; Pang, Myung-Geol

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자료유형: 학술저널

저자정보: Lee, June-Sub (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Park, Yoo-Jin (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Kim, Jin (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Rahman, Md. Saidur (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Kwon, Woo-Sung (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Yoon, Sung-Jae (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) You, Young-Ah (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University) Pang, Myung-Geol (Department of Animal Science and Technology, School of Bioresource & Bioscience, Chung-Ang University)

저널정보: 한국동물번식학회 한국동물번식학회지 한국동물번식학회지 제37권 제4호

발행연도: 2013.1

수록면: 169 - 174 (6page)

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Sperm capacitation refers to polymerization of filamentous (F)-actin from globular (G)-actin. While the role of actin-related protein 2/3 (Arp2/3) complex in actin polymerization is well appreciated, the underlying mechanism(s) and its relationship with capacitation are poorly understood. Therefore, to evaluate the potential role of Arp2/3 complex on capacitation, bovine spermatozoa were incubated with multiple doses (1, 10 and $100{\mu}M$) of CK-636, an inhibitor of Arp2/3 complex with heparin. The cellular localization of the Arp2/3 complex in spermatozoa was identified by immunohistochemistry, whereas western blot was also applied to detect the protein tyrosine phosphorylation of sperm proteins. Additionally, sperm motility and kinematic parameters were evaluated using a computer-assisted sperm analysis system. CK-636 resulted in significant changes in the ratio of Arp2/3 complex localization between acrosome and equatorial region of the spermatozoa. Short-term exposure of spermatozoa to $100{\mu}M$ of CK-636 significantly decreased sperm motility, however a non-detectable effect on protein tyrosine phosphorylation was observed during capacitation. On the basis of these results, we propose that Arp2/3 complex is associated with morphological changes during capacitation and compromised sperm motility.

#Arp2/3 complex #CK-636 #Sperm capacitation #Actin polymerization #Bovine spermatozoa

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